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Trends in Comparative Biochemistry & Physiology   Volumes    Volume 4 
Structure and function of mammalian α-L-fucosidases
Jack A. Alhadeff
Pages: 105 - 118
Number of pages: 14
Trends in Comparative Biochemistry & Physiology
Volume 4 

Copyright © 1998 Research Trends. All rights reserved

Mammalian α-L-fucosidases (EC are a ubiquitous group of multimeric lysosomal glycosidases involved in the degradation of a diverse collection of fucose-containing oligosaccharides, glycolipids and glycoproteins. The importance of this enzyme in mammalian metabolism is evidenced by deficiency or absence of enzymatic activity leading to the fatal genetic disease fucosidosis. Mammalian α-L-fucosidases are sialoglycoproteins and the presence and amount of sialic acid contribute to producing multiple isoforms which can differ in various species as well as in different tissues within a given species. These enzymes are closely related structurally as indicated by immunochemical cross-reactivity and cloning studies. α-L-Fucosidases have similar kinetic properties (pH optimum, Km values) with synthetic substrates and exhibit broad substrate specificity on natural substrates. Numerous linkages (α1 -2, α1-3, α1-4, α1-6) of L-fucose, primarily to galactose and N-acetylglucosamine, can be hydrolyzed with preference shown for fucose in α1-2 linkage to galactose in low molecular-weight, water soluble compounds. Recent studies have provided evidence for a novel, plasma membrane-associated sperm fucosidase which may be involved in sperm-egg interactions and/or fertilization.
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